Research workbench
Structural basis for phosphatidylinositol phosphate kinase type I- gamma binding to talin at focal adhesions
Analyse Structural basis for phosphatidylinositol phosphate kinase type I- gamma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Y19
- Type
- protein
- Length
- 1,218 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphatidylinositol-4-phosphate 5-kinase, type 1 gamma; Talin 1
- UniProt
- O70161, P26039
- Pockets
- 6 · best druggability 0.50
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K | Phosphatidylinositol-4-phosphate 5-kinase, type 1 gamma | protein | 11 | 27% helix, 27% strand | O70161 |
| B, D, F, H, J, L | Talin 1 | protein | 192 | 42% helix, 21% strand | P26039 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 260 | 0.50 | 0.74 | 39 | empty |
| 2 | 100 | 0.40 | 0.76 | 22 | empty |
| 3 | 53 | 0.33 | 0.77 | 15 | empty |
| 4 | 58 | 0.30 | 0.75 | 18 | empty |
| 5 | 50 | 0.28 | 0.75 | 17 | empty |
Interfaces
18 interfaces between chains.
- E–H · 566 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 561 Ų buried · 8 hydrogen bonds · protein-protein
- A–D · 557 Ų buried · 7 hydrogen bonds · protein-protein
- F–G · 554 Ų buried · 6 hydrogen bonds · protein-protein
- J–K · 553 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1Y19 · Structural basis for phosphatidylinositol phosphate kinase type I-gamma binding to talin… · the same entry in another collection · chain L against L, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O70161
- Every structure of UniProt P26039
- Elsewhere: RCSB PDB 1Y19 · PDBe 1Y19 · UniProt O70161 · UniProt P26039
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